In addition to cleaving peplides, chymotrypsin can akso catalyze the hydrołysis of certain small organic molecules such as acetanides (below). Based on the data given below, which compound, 4-melhyl- or 4-chloroacetanilide, is the better substrate (L.e., the more specific substrate) for chymotrypsin? Briefly explain how the data indicate that this amide is the better substrate for the enzyme. Cormpound X= CH, X= CI Kae (min") 5.22 K (mM) 13 0.84 0.67

Biochemistry
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ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
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Chapter1: Biochemistry: An Evolving Science
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In addition to cleaving peplides, chymotrypsin can also catalyze the Irydrolysis of certain smal
organic molecules such as acetanīlides (below).
Based on the data given below, which compound, 4-melhyl- or 4-chloroacelanilide, is the better substrate
(L.e., the more specific substrate) for chymotrypsin? Briefly explain how the data indicate that this amide is
the better substrate for the enzyme.
Compound
X= CH,
Ka (min")
5.22
K. (mM)
13
X= CI
0.84
0.67
As wilh peptides, chymolrypsin-catalyzed hydrolysis of acetanilides uses the hydroxyl group of a serine to
form an intermediate containing a covalent bond between the enzyme and a portion of the substrate.
Using E-OH to represent the enzyme, draw the structure of the covalent enzyme-intermediate complex for
the reaction of chymotrypsin with acetanilide (Ph = benzene ring).
Transcribed Image Text:In addition to cleaving peplides, chymotrypsin can also catalyze the Irydrolysis of certain smal organic molecules such as acetanīlides (below). Based on the data given below, which compound, 4-melhyl- or 4-chloroacelanilide, is the better substrate (L.e., the more specific substrate) for chymotrypsin? Briefly explain how the data indicate that this amide is the better substrate for the enzyme. Compound X= CH, Ka (min") 5.22 K. (mM) 13 X= CI 0.84 0.67 As wilh peptides, chymolrypsin-catalyzed hydrolysis of acetanilides uses the hydroxyl group of a serine to form an intermediate containing a covalent bond between the enzyme and a portion of the substrate. Using E-OH to represent the enzyme, draw the structure of the covalent enzyme-intermediate complex for the reaction of chymotrypsin with acetanilide (Ph = benzene ring).
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